Evidence map›Paper›PMID 30366211›Full record

ArticleJournal of chromatography. B, Analytical technologies in the biomedical and life sciences2018

Binding studies based on ultrafast affinity extraction and single- or two-column systems: Interactions of second- and third-generation sulfonylurea drugs with normal or glycated human serum albumin.

Bao Yang, Xiwei Zheng, David S Hage

Abstract read
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In one paragraph

Article in Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.6field-weighted citation impact, top 33% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Analysis of the binding of warfarin to glyoxal- and methylglyoxal-modified human serum albumin by ultrafast affinity extraction.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2022
    Article
  5. Evaluation of microcolumn stability in ultrafast affinity extraction for binding and rate studies.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2021
    Article
  6. Review
  7. Article
  8. Affinity chromatography: A review of trends and developments over the past 50 years.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2020
    Review
  9. Kinetic Analysis by Affinity Chromatography.Frontiers in chemistry · 2019
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Bao YangChemistry Department, University of Nebraska, Lincoln, NE 68588-0304, USA.
Xiwei ZhengChemistry Department, University of Nebraska, Lincoln, NE 68588-0304, USA.
David S HageChemistry Department, University of Nebraska, Lincoln, NE 68588-0304, USA. Electronic address: dhage1@unl.edu.
University of Nebraska–Lincoln · US

Funding

CHROMATOGRAPHIC STUDIES OF FUNCTIONAL PROTEOMICSR01DK069629 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI HAGE, DAVID S · 2006 to 2017
$1.8M
NIDDK NIH HHS R01 DK069629
6 · The paper itself

Abstract

Ultrafast affinity extraction was evaluated and used with microcolumns containing human serum albumin (HSA) to measure the global affinity constants and dissociation rate constants for several second- and third-generation sulfonylurea drugs with solution-phase normal HSA or glycated HSA. Glibenclamide, glimepiride and glipizide were used as model drugs for this work. Both single- and two-column systems were considered for the analysis of global affinities for the model drugs. These methods were optimized with respect to the flow rates, column sizes and sample residence times that were employed with each drug for ultrafast affinity extraction. Data acquired with single-column systems were further utilized to estimate the dissociation rate constants for normal HSA and glycated HSA with the given drugs. The binding constants obtained by the single- and two-column systems showed good agreement with each other and with values obtained from the literature. Use of a single-column system indicated that levels of glycation found in controlled or advanced diabetes resulted in a 18-44% decrease in the overall binding strength of the model drugs with HSA. Although the two-column system allowed work with smaller free drug fractions and clinically-relevant drug/protein concentrations, the single-column system required less protein, provided better precision, and was easier to use in binding studies.

Indexed as

Chromatography, AffinityDiabetes MellitusGlycosylationHumansHypoglycemic AgentsProtein BindingSerum Albumin, HumanSulfonylurea CompoundsHypoglycemic AgentsSerum Albumin, HumanSulfonylurea CompoundsDiabetesDrug-protein bindingGlycationHuman serum albuminSulfonylurea drugsUltrafast affinity extraction

Identifiers

PMID30366211
PMCPMC6251404
OpenAlexW2896558616

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.